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🖤 MT6310 > [lab] proteins > Flashcards

[lab] proteins Flashcards

1
Q

most abundant biomolecule in all cells

A

protein

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2
Q

binds amino acids to another amino acid, forming proteins

A

peptide bond

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3
Q

nonpolar aliphatic r groups

A

GAVLIPM

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4
Q

aromatic r group

A

WYF

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5
Q

positively charged group

A

RHK

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6
Q

negatively charged r group

A

ED

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7
Q

polar uncharged group

A

SCTNQ

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8
Q

sequence of amino acid residues that serves as the backbone of a peptide chain or protein

A

primary structure

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9
Q

regular, repeating folding patterns

A

secondary structure

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10
Q

a-helix and b-pleated sheets

A

secondary structure

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11
Q

rod-like structure; h-bonds parallel to axis

A

a-helix

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12
Q

typically amphiphilic

A

a-helix

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13
Q

polypeptide chains arranged side by side; h bonds between chain

A

b-pleated sheets

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14
Q

may be parallel or antiparallel

A

b-pleated sheets

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15
Q

more stable b-pleated sheets

A

antiparallel

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16
Q

protein fold in 3 dimensions; overall folding of domains

A

tertiary structure

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17
Q

specific overall shape of a protein

A

tertiary structure

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18
Q

cross links between r groups of amino acid in chain

A

tertiary structure

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19
Q

interaction between different polypeptide chains to produce an oligometric structure

A

quaternary structure

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20
Q

aggregates of two or more protein chains connected by weak non-covalent interactions

A

quaternary structure

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21
Q

proteins with two or more chains

A

quaternary structure

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22
Q

classification of proteins

A

(CBSS)
according to composition
according to biological function
according to shape
according to solubility

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23
Q

yield only amino acids upon hydrolysis

A

simple proteins

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24
Q

simple proteins + non-protein substances

A

conjugated proteins

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25
Q

biological functions of proteins

A

(NETSCDR)
nutrient & storage
enzymes
transport
structural
contractile & motile
defense
regulatory

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26
Q

polypeptide chain/s folded into spherical /globular shape

A

globular proteins

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27
Q

soluble in aqueous system

A

globular proteins

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28
Q

polypeptide chains arranged in long strands or sheets

A

fibrous proteins

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29
Q

water insoluble protein

A

fibrous proteins

30
Q

protein classification according to solubility

A

(AGPAG)
albumin
globulin
prolamin
albuminoids/scleroproteins
glutelin

31
Q

protein soluble in water and dilute aqueous solutions

A

albumin (plasma)

32
Q

protein soluble in salt and dilute solutions; insoluble in water

A

globulins (serum)

33
Q

protein soluble in dilute solutions of acids and bases; insoluble in neutral solvents

A

glutelins (flour)

34
Q

store protein in plants; soluble in 50-90% alcohol; insoluble in water, neutral solvents, or absolute alcohol

A

prolamins

35
Q

insoluble in most ordinary solvents

A

albuminoids/scleroproteins

36
Q

loss of three dimensional structure sufficient to cause of loss of function

A

protein denaturation

37
Q

leads to primary structure

A

denaturation

38
Q

leads to destruction of all structure

A

hydrolysis

39
Q

denaturing agents

A

(SHARBOTD)
salts
heavy metals
acid (strong)
reducing agents
base (strong)
organic solvent
temperature
detergents

40
Q

types of denaturation

A

irreversible & reversible

41
Q

uses strong acid / base + high temperature; product: amino acid

A

complete hydrolysis

42
Q

uses enzymes called protease; product: mixture of amino acids and oligopeptides

A

incomplete / partial hydrolysis

43
Q

most commonly used reagent for acid hydrolysis

A

6N HCl

44
Q

reagent for alkaline hydrolysis

A

NaOH or KOH

45
Q

partially destroyed amino acid in acid hydrolysis

A

CY

46
Q

completely destroyed amino acid in acid hydrolysis

A

W

47
Q

incompletely liberated amino acid in acid hydrolysis

A

VI

48
Q

racemized and destroyed amino acid in acid hydrolysis

A

ST

49
Q

in acid hydrolysis N+Q is converted into

A

D+E

50
Q

advantage of alkaline hydrolysis

A

W not destroyed

51
Q

disadvantage of alkaline hydrolysis

A

RNQS are destroyed

52
Q

___ are needed to facilitate the hydrolysis of peptide bonds

A

catalysts

53
Q

enzymes that hydrolyze peptide binds at specific sites

A

protease

54
Q

advantage of incomplete / partial hydrolysis

A

amino acids are not affected

55
Q

presence of proteolytic enzymes result to partial / selective hydrolysis of polypeptide to yield a mixture of peptide fragments

A

enzymatic hydrolysis

56
Q

requires certain temperature and ph conditions for optimum activity of enzymes

A

incomplete / partial hydrolysis

57
Q

exopeptidases

A

carboxypeptidase a
carboxypeptidase b
aminopeptidase

58
Q

c-terminal residues

A

carboxypeptidases

59
Q

n-terminal residues

A

aminopeptidases

60
Q

carboxypeptidase a

A

c-terminal residues except R,K,P

61
Q

carboxypeptidase b

A

except R or K at C-terminus

62
Q

aminopeptidase

A

most n-terminal except when p is the next residue

63
Q

endopeptidases

A

trypsin
chymotrypain
papain

64
Q

trypsin

A

c side R K

65
Q

chymotrypsin

A

c side W Y F

66
Q

papain

A

c side of hydrophobic / aromatic r groups

67
Q

properties of proteins to consider in separation / purification of proteins

A

(CASIM)
charge
affinity to ligand
solubility
isoelectric point
molecular size/shape

68
Q

procedure in which the ph of the protein mixture is adjusted to the pI of the protein to be isolated to selectively minimize its solubility

A

isoelectric precipitation

69
Q

change in ionic strength

A

salting in / salting out

70
Q

relationship of salt concentration and solubility

A

inverse (high salt conc. = low solubility; vice versa)

🖤 MT6310 (4 decks)

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